蛋白质二硫键异构酶的研究从六十年代发现以来一直比较活跃。
The studying of Protein Disulfide Isomerase is active since it was discovered in 60th.
正常的链接是二硫键，可以被热度和酸度变化所破坏，导致蛋白质失去三维结构。
The normal kind of bonds - disulphide bonds - can be broken by changes in heat and acidity, causing proteins to lose their 3d structure.
集中介绍了IGF1的三维结构、IGF 1与相关受体和结合蛋白的结合区以及二硫键在蛋白质折叠中的重要作用。
It is concentrated on the three dimensional structure of human IGF1, and the combining regions between IGF1 and relative receptors and binding proteins.
应用这个方法对蛋白质结构的二硫键进行了预测并取得了良好的结果。
This method has being used to predict disulfide bonding in protein structure and a fine result has been got.
对近紫外圆二色作为光谱探针，研究蛋白质中芳香氨基酸残基、二硫键微环境的变化作了简单介绍。
The method that near-UV CD spectrum served as useful probes to provide the information of dissymmetric environments of aromatic residues and disulfur bonds is also introduced briefly.
对近紫外圆二色作为光谱探针，研究蛋白质中芳香氨基酸残基、二硫键微环境的变化作了简单介绍。
The method that near-UV CD spectrum served as useful probes to provide the information of dissymmetric environments of aromatic residues and disulfur bonds is also introduced briefly.
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